Any feedback?
Information on EC 1.7.1.15 - nitrite reductase (NADH) and Organism(s) Escherichia coli and UniProt Accession P0A9I8
for references in articles please use BRENDA:EC1.7.1.15Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.7.1.15 nitrite reductase (NADH)IUBMB Comments
An iron-sulfur flavoprotein (FAD) containing siroheme. This prokaryotic enzyme is specific for NADH. In addition to catalysing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyse the 2-electron reduction of hydroxylamine to ammonia. cf. EC 1.7.1.4, nitrite reductase [NAD(P)H].
Specify your search results
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nadh-dependent nitrite reductase, nirbd, nadh-nitrite reductase, nasde, assimilatory nadh-nitrite reductase, nadh-dependent nitrite oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NADH-dependent nitrite reductase
-
-
NADH-nitrite oxidoreductase
nirB
nirD
-
-
-
-
nitrite reductase (reduced nicotinamide adenine dinucleotide)
-
-
-
-
NADH-nitrite oxidoreductase
-
-
-
-
nirB
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ammonia:NAD+ oxidoreductase
An iron-sulfur flavoprotein (FAD) containing siroheme. This prokaryotic enzyme is specific for NADH. In addition to catalysing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyse the 2-electron reduction of hydroxylamine to ammonia. cf. EC 1.7.1.4, nitrite reductase [NAD(P)H].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
-
-
-
-
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
-
-
-
-
?
additional information
?
-
NirB, NirD polypeptides are essential for NADH-dependent nitrite reductase activity
-
-
?
additional information
?
-
-
NirB, NirD polypeptides are essential for NADH-dependent nitrite reductase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
-
the enzyme contains 5 Fe atoms and 4 acid-labile S atoms per subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCN
-
although 1 mM KCN completely inhibits hydroxylamine reduction, it does not inhibit the reduction of K3Fe(CN)6 and only decreases the rate of cytochrome c reduction by 12%
NAD+
-
NAD+ shows mixed product inhibition with respect to NADH and mixed or uncompetitive inhibition with respect to hydroxylamine
nitrite
-
nitrite decrease the rate of NADH-dependent reduction of cytochrome c by 77% and that of Fe(CN)63- by 90%
p-chloromercuribenzoate
-
the reduction of cytochrome c, K3Fe(CN)6 and hydroxylamine is completely inhibited (more than 99%) by 0.02 mM p-chloromercuribenzoate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
at 0.5 mM NAD+, the apparent maximum velocity is 2.3times higher for 0.1 mM cytochrome c as substrate than for 100 mM hydroxylamine
NAD+
-
the apparent maximum velocity with NADH as varied substrate increases as the NAD+ concentration increases from 0.05 to 0.7 mM with 1 mM nitrite or 100 mM hydroxylamine as oxidized substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0488
NADH
-
with cytochrome c as cosubstrate, apparent value, at pH 8.0 and 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is necessary for nitrate/nitrite assimilation but also either detoxify nitrite or carries out fermentative ammonification in support of anaerobic catabolism. The enzyme confers a significant benefit during fermentative growth that reflects fermentative ammonification rather than detoxification. Fermentative ammonification by the enzyme allows for the energetically favorable fermentation of glucose to formate and acetate
physiological function
-
the enzyme is a key contributor to regulation of the nitric oxide level during nitrate respiration
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
88000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 30
the nitrite reductase activities of concentrated mixtures prepared on ice do not increase during subsequent incubation at 30°C or at 4°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM nitrite and 5O mM hydroxylamine are equally effective in decreasing the loss of activity after 24h at 40°C from 40% to 10%. No increase in catalytic activity is detected when enzyme is pre-incubated for 15 min with either of these substrates, even when NAD+ is omitted from the assay mixture
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified in the presence of 1 mM NO2- and 0.01 mM FAD by ammonium sulfate precipitation, DEAE-cellulose column chromatography, DEAE-Sephadex gel filtration, and Sephadex G-25 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
MacDonald, H.; Cole, J.
Molecular cloning and functional analysis of the cysG and nirB genes of Escherichia coli K12, two closely-linked genes required for NADH-dependent nitrite reductase activity
Mol. Gen. Genet.
200
328-334
1985
Escherichia coli
Cammack, R.; Jackson, R.H.; Cornish-Bowden, A.; Cole, J.A.
Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12
Biochem. J.
207
333-339
1982
Escherichia coli
Jackson, R.H.; Cole, J.A.; Cornish-Bowden, A.
The steady-state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12
Biochem. J.
199
171-178
1981
Escherichia coli
Jackson, R.H.; Cornish-Bowden, A.; Cole, J.A.
Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12
Biochem. J.
193
861-867
1981
Escherichia coli
Jackson, R.H.; Cole, J.A.; Cornish-Bowden, A.
The steady state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12. The reduction of single-electron acceptors
Biochem. J.
203
505-510
1982
Escherichia coli
Harborne, N.R.; Griffiths, L.; Busby, S.J.; Cole, J.A.
Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon
Mol. Microbiol.
6
2805-2813
1992
Escherichia coli (P0A9I8), Escherichia coli
Wang, X.; Tamiev, D.; Alagurajan, J.; DiSpirito, A.A.; Phillips, G.J.; Hargrove, M.S.
The role of the NADH-dependent nitrite reductase, Nir, from Escherichia coli in fermentative ammonification
Arch. Microbiol.
201
519-530
2019
Escherichia coli
EXTERNAL LINKS (specific for EC-Number 1.7.1.15)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
